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O28440

- ASPD_ARCFU

UniProt

O28440 - ASPD_ARCFU

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Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.UniRule annotation

Catalytic activityi

L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111NAD; via amide nitrogenUniRule annotation
Binding sitei162 – 1621NADUniRule annotation
Active sitei189 – 1891UniRule annotation

GO - Molecular functioni

  1. aspartate dehydrogenase activity Source: UniProtKB-EC
  2. NAD binding Source: UniProtKB-HAMAP
  3. NADP binding Source: UniProtKB-HAMAP
  4. oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Source: UniProtKB-HAMAP

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-HAMAP
  2. NADP catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-1873-MONOMER.
SABIO-RKO28440.
UniPathwayiUPA00253; UER00456.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable L-aspartate dehydrogenaseUniRule annotation (EC:1.4.1.21UniRule annotation)
Gene namesi
Name:nadXUniRule annotation
Ordered Locus Names:AF_1838
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
ProteomesiUP000002199: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236Probable L-aspartate dehydrogenasePRO_0000144894Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224325.AF1838.

Structurei

Secondary structure

1
236
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi10 – 2112Combined sources
Beta strandi25 – 306Combined sources
Beta strandi39 – 424Combined sources
Helixi43 – 464Combined sources
Beta strandi52 – 565Combined sources
Helixi60 – 7213Combined sources
Beta strandi76 – 805Combined sources
Helixi82 – 865Combined sources
Helixi88 – 10114Combined sources
Beta strandi105 – 1073Combined sources
Helixi115 – 1206Combined sources
Helixi122 – 1243Combined sources
Beta strandi125 – 13511Combined sources
Helixi136 – 1383Combined sources
Beta strandi143 – 1497Combined sources
Helixi150 – 1567Combined sources
Helixi162 – 17110Combined sources
Beta strandi176 – 1838Combined sources
Beta strandi185 – 19511Combined sources
Beta strandi198 – 2069Combined sources
Beta strandi212 – 2165Combined sources
Helixi217 – 23115Combined sources
Beta strandi232 – 2354Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DC1X-ray1.90A/B1-236[»]
ProteinModelPortaliO28440.
SMRiO28440. Positions 1-236.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO28440.

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1712.
KOiK06989.
OMAiECAGHSA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01265. NadX.
InterProiIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR022487. Asp_DH_arc.
IPR020626. Asp_DH_prok.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF005227. Asp_dh_NAD_syn. 1 hit.
TIGRFAMsiTIGR03855. NAD_NadX. 1 hit.

Sequencei

Sequence statusi: Complete.

O28440-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLVGLIGYGA IGKFLAEWLE RNGFEIAAIL DVRGEHEKMV RGIDEFLQRE
60 70 80 90 100
MDVAVEAASQ QAVKDYAEKI LKAGIDLIVL STGAFADRDF LSRVREVCRK
110 120 130 140 150
TGRRVYIASG AIGGLDAIFS ASELIEEIVL TTRKNWRQFG RKGVIFEGSA
160 170 180 190 200
SEAAQKFPKN LNVAATLSIA SGKDVKVRLV ADEVEENIHE ILVRGEFGEM
210 220 230
EIRVRNRPMR ENPKTSYLAA LSVTRILRNL KEGLVV
Length:236
Mass (Da):26,208
Last modified:January 1, 1998 - v1
Checksum:i29218ACC7F919F52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89415.1.
PIRiE69479.
RefSeqiNP_070664.1. NC_000917.1.
WP_010879332.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB89415; AAB89415; AF_1838.
GeneIDi1485059.
KEGGiafu:AF1838.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89415.1 .
PIRi E69479.
RefSeqi NP_070664.1. NC_000917.1.
WP_010879332.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DC1 X-ray 1.90 A/B 1-236 [» ]
ProteinModelPortali O28440.
SMRi O28440. Positions 1-236.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224325.AF1838.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB89415 ; AAB89415 ; AF_1838 .
GeneIDi 1485059.
KEGGi afu:AF1838.

Phylogenomic databases

eggNOGi COG1712.
KOi K06989.
OMAi ECAGHSA.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci AFUL224325:GJBC-1873-MONOMER.
SABIO-RK O28440.

Miscellaneous databases

EvolutionaryTracei O28440.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_01265. NadX.
InterProi IPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR022487. Asp_DH_arc.
IPR020626. Asp_DH_prok.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF005227. Asp_dh_NAD_syn. 1 hit.
TIGRFAMsi TIGR03855. NAD_NadX. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Entry informationi

Entry nameiASPD_ARCFU
AccessioniPrimary (citable) accession number: O28440
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.UniRule annotation

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3